Archives February 2022

Cusabio Salmonella typhimurium Recombinant

Abstract

The HIV/AIDS epidemic continues to be a global health problem, especially in sub-Saharan Africa. Therefore, an effective HIV-1 vaccine is urgently needed to mitigate this ever-expanding problem. Since HIV-1 infects its host through the mucosal surface, a vaccine against the virus must elicit both mucosal and systemic immune responses. Oral attenuated recombinant Salmonella vaccines offer this potential to deliver HIV-1 antigens to the mucosal and systemic compartments of the immune system.

To date, a number of preclinical studies have been conducted, in which HIV-1 Gag, a highly conserved viral antigen possessing T- and B-cell epitopes, has been successfully delivered by recombinant Salmonella typhimurium vaccines, and in most cases, HIV-specific immune responses were induced. In this review, the potential use of Salmonella enterica serovar Typhimurium as a live vaccine vector for HIV-1 Gag is explored.

Keywords: Salmonella, vaccine, vector, HIV-1 Gag, immune response

Purity: >85% (SDS-PAGE)

Target Names: cheY

Uniprot No.: P0A2D5

Alternative names: cheY; STM1916; CheY chemotaxis protein

Species: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Expression Region: 2-129

Protein length: Total length of the mature protein

Label information

The following labels are available.

  • N-terminus His-tagged
  • Without tags
  • The type of label will be determined during the production process. If you have specified a tag type, let us know and we will develop the specified tag preferentially.

Form: Lyophilized powder

Buffer before lyophilization: Tris/PBS based buffer, 6% trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged before opening to bring the contents to the bottom. Reconstitute protein in sterile deionized water at a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and an aliquot for long-term storage at -20℃/-80℃. Our final default glycerol concentration is 50%. Customers could use it for reference.

Storage Conditions

Store at -20°C/-80°C upon receipt, need to be aliquoted for multiple uses. Avoid repeated cycles of freezing and thawing.

Shelf life

Shelf life is related to many factors, storage condition, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of the liquid form is 6 months at -20°C/-80°C. The shelf life of the lyophilized form is 12 months at -20°C/-80°C.

Delivery time

The delivery time may differ depending on the way or location of purchase, consult your local distributors for the specific delivery time.

Note: All of our proteins are shipped with regular blue ice packs by default. If you request shipping with dry ice, please contact us in advance and additional fees will be charged.

Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Cusabio Saccharomyces cerevisiae Recombinant

Introduction

The production of recombinant therapeutic proteins is one of the rapidly growing areas of molecular medicine and currently plays an important role in the treatment of various diseases. Yeasts are unicellular eukaryotic microbial host cells that offer unique advantages in the production of biopharmaceutical proteins. Yeasts are capable of robust growth on simple media, readily adapt to genetic modifications, and incorporate post-translational modifications typical of eukaryotes.

Saccharomyces cerevisiae Recombinant is a traditional baker’s yeast that has been used as an important host for the production of biopharmaceuticals; however, several unconventional yeast species, including Hansenula polymorpha, Pichia pastoris, and Yarrowia lipolytica, have gained increasing attention as alternative hosts for the industrial production of recombinant proteins. In this review, we address established and emerging genetic tools and host strains suitable for recombinant protein production in various yeast expression systems, with a particular focus on current efforts toward synthetic biology, approaches in the development of yeast cell factories. for the production of therapeutic recombinant proteins.

Polyketide synthases

In nature, polyketides are formed enzymatically by consecutive Claisen condensation reactions of short-chain acyl derivatives. At the biochemical level, polyketide assembly is very reminiscent of fatty acid biosynthesis, although it involves a greater variety of initiator and extender units. Furthermore, it shows greater flexibility in the reductive processing of these building blocks. Due to these peculiarities, polyketides exhibit enormous structural diversity, ranging from polyenes, polyethers and enediynes to macrolides, phenolic and polycyclic aromatic compounds.

The enzymes, which are responsible for the biosynthesis of these molecules, are called polyketide synthases (PKS). According to their architecture, they can be divided into three classes. Type I PKS are large, modularly organized proteins of microbial origin. They have multiple catalytic domains with specific functions. While most type I bacterial PKSs follow a logic of sequential assembly, their fungal counterparts tend to operate repetitively. The latter is also true for type II PKSs, which form monofunctional protein complexes. Until now, type II PKSs have only been found in a few prokaryotic groups, for example, in actinomycetes bacteria.

In contrast, type III PKSs represent the most widely distributed class of all PKSs with known members from bacteria, fungi, (micro)algae, and plants. Structurally, they are much smaller and less complex than the other two PKS classes. They consist of a homodimeric ketosynthase, which governs the entire assembly process, from substrate discrimination to chain elongation and product release. In the following, we will focus exclusively on the assembly mechanisms of type I PKS. Readers who wish to learn more about type II and type III PKS are referred to the reviews by Wang et al. and Shimizu et al.

Results and Discussion

Evaluation of target genes in protein secretion and retention.

Based on a list of mutated genes obtained from our previous study (18), genes involved in secretory and trafficking pathways (such as ECM3, EMC1, ERV29, GOS1, VPS5, TDA3, COG5, and CNS2), genes with similar functions appearing in Different strains (HDA2 and HDA3) and genes with a missense mutation of enriched GO terms (such as TAN1 from tRNA processing, PGM2 from carbohydrate metabolic process and PXA1 from lipid transport) were selected for evaluating its association with protein secretion and retention using single gene deletions.

To allow an initial selection of these different targets, we used the BY4742 strain background for which a unique gene deletion library is available, but consistent with our previous study, we used amylase as the model protein. Amylase production varied in BY4742 strains with a single gene deletion; some had increased amylase secretion and some had reduced amylase secretion compared with the reference strain. In addition to changes in amylase yield, the intracellular amylase ratio was also found to be altered by gene deletion.

Cusabio Transport Recombinants

Abstract

Solar cells using perovskite as a semiconductor pigment have recently attracted great interest due to their remarkable solar-to-electrical energy conversion efficiencies and ease of processing. In this direction, various device architectures and materials have been employed, and attempts have been made to elucidate the underlying operating principles. However, the factors that govern the performance of perovskite devices are still obscure.

For example, interpretation of electrochemical impedance spectroscopy (EIS) is not straightforward and the complexity of equivalent circuits makes it difficult to identify transport and recombination mechanisms in devices, especially those that determine device performance. Here we carry out a complete and complementary characterization of perovskite solar cells using a series of small perturbation techniques: EIS and intensity-modulated photocurrent and photovoltage spectroscopy (IMPS/IMVS). Using IMPS allowed us to identify two transport times separated by 2 orders of magnitude and with opposite voltage dependencies.

For recombination, a good agreement was found between the lifetimes obtained by IMVS and EIS. The feature associated with recombination and charge accumulation in an impedance spectrum was experimentally identified through correlation with the IMVS response. This correlation paves the way to reconstruct the current-voltage curve using a continuity equation model for transport and recombination in the working device. The adopted methodology demonstrates that complementary techniques facilitate the interpretation of EIS results in perovskite solar cells, allowing us to identify transport recombination mechanisms and providing new insights into the steps that determine efficiency.

Purity: >85% (SDS-PAGE)

Destination Names: Mert

Uniprot No.: P13112

Alternative Names: merT; mercury transporter protein Mert; Mercury ion transport protein

Species: Serratia marcescens

Protein length: Partial

Label information

The following labels are available.

  • N-terminus His-tagged
  • Without tags
  • The type of label will be determined during the production process. If you have specified a tag type, let us know and we will develop the specified tag preferentially.

Form: Lyophilized powder

Buffer before lyophilization: Tris/PBS based buffer, 6% trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged before opening to bring the contents to the bottom. Reconstitute protein in sterile deionized water at a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and an aliquot for long-term storage at -20℃/-80℃. Our final default glycerol concentration is 50%. Customers could use it for reference.

Storage Conditions

Store at -20°C/-80°C upon receipt, need to be aliquoted for multiple uses. Avoid repeated cycles of freezing and thawing.

Shelf life

Shelf life is related to many factors, storage condition, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of the liquid form is 6 months at -20°C/-80°C. The shelf life of the lyophilized form is 12 months at -20°C/-80°C.

Delivery time

The delivery time may differ depending on the form or location of purchase, consult your local distributors for the specific delivery time.

Note: All of our proteins are shipped with regular blue ice packs by default. If you request shipping with dry ice, please contact us in advance and additional fees will be charged.

Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Freight transport and load recombination

Charge carrier transport and carrier recombination govern the operation of all electronic devices, including those that use organic semiconductors. Therefore, understanding charge transport and charge recombination in organic semiconductors is a prerequisite for successfully designing future high-performance organic electronic devices. In our group, we study the transport of charge carriers through the fabrication of field-effect transistors and what are known as single-carrier devices.

Understanding the energy of organic materials allows us to isolate either hole or electron transport by choosing electrode materials with the correct work functions relative to the boundary energy levels of a given organic compound. Analysis of the current-voltage characteristics of these devices provides information on how fast these charge carriers are transported through organic material and whether the organic material under investigation possesses the right properties to be used in high-performance organic solar cells. , field-effect transistors, or light-emitting diodes.

We employ a variety of techniques to understand recombination mechanisms in organic semiconductors. The study of double carrier devices allows us to investigate the process of recombination of holes with electrons. This process is a fundamental loss mechanism in organic solar cells, but it is essential for the operation of light-emitting diodes. Furthermore, we investigate recombination mechanisms by observing photoluminescence, electroluminescence, quantum efficiency, and impedance response of organic electronic devices as a function of temperature and excitation energy.